Results 31 to 40 of about 142,894 (282)

The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site [PDF]

open access: yes, 2008
Ribosome biogenesis in eukaryotes requires the participation of a large number of ribosome assembly factors. The highly conserved eukaryotic nucleolar protein Nep1 has an essential but unknown function in 18S rRNA processing and ribosome biogenesis.
Wöhnert, Jens   +8 more
core   +1 more source

The Bowen–Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Psi1191 in yeast 18S rRNA [PDF]

open access: yes, 2010
The Nep1 (Emg1) SPOUT-class methyltransferase is an essential ribosome assembly factor and the human Bowen–Conradi syndrome (BCS) is caused by a specific Nep1D86G mutation. We recently showed in vitro that Methanocaldococcus jannaschii Nep1 is a sequence-
Valeska Schilling   +27 more
core   +1 more source

Rational Extension of the Ribosome Biogenesis Pathway Using Network-Guided Genetics [PDF]

open access: yes, 2009
Biogenesis of ribosomes is an essential cellular process conserved across all eukaryotes and is known to require >170 genes for the assembly, modification, and trafficking of ribosome components through multiple cellular compartments.
Edward M. Marcotte   +19 more
core   +1 more source

Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA [PDF]

open access: yes, 2012
Ribosomal RNA undergoes various modifications to optimize ribosomal structure and expand the topological potential of RNA. The most common nucleotide modifications in ribosomal RNA (rRNA) are pseudouridylations and 2'-O methylations (Nm), performed by H ...
Sharma, Sunny   +5 more
core   +1 more source

Cell autonomous and non-autonomous consequences of deviations in translation machinery on organism growth and the connecting signalling pathways

open access: yesOpen Biology, 2022
Translation machinery is responsible for the production of cellular proteins; thus, cells devote the majority of their resources to ribosome biogenesis and protein synthesis. Single-copy loss of function in the translation machinery components results in
Agustian Surya, Elif Sarinay-Cenik
doaj   +1 more source

Impairing the production of ribosomal RNA activates mammalian target of rapamycin complex 1 signalling and downstream translation factors [PDF]

open access: yes, 2014
Ribosome biogenesis is a key process for maintaining protein synthetic capacity in dividing or growing cells, and requires coordinated production of ribosomal proteins and ribosomal RNA (rRNA), including the processing of the latter.
Proud, C.   +17 more
core   +1 more source

Genome-wide RNAi Screening Identifies Protein Modules Required for 40S Subunit Synthesis in Human Cells

open access: yesCell Reports, 2015
Ribosome biogenesis is a highly complex process requiring many assisting factors. Studies in yeast have yielded comprehensive knowledge of the cellular machinery involved in this process.
Lukas Badertscher   +12 more
doaj   +1 more source

Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase [PDF]

open access: yes, 2008
In yeast, three small nucleolar RNAs (snoRNAs) are essential for the processing of pre-ribosomal RNA—U3, U14 and snR30—whereas 72 non-essential snoRNAs direct site-specific modification of pre-rRNA. We applied a quantitative screen for alterations in the
Martin Kos   +6 more
core   +1 more source

The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14 [PDF]

open access: yes, 2005
One of the proteins identified as being involved in ribosome biogenesis by high-throughput studies, a putative P-loop-type kinase termed Fap7 (YDL166c), was shown to be required for the conversion of 20S pre-rRNA to 18S rRNA.
Nandineni, Madhusudan R   +2 more
core   +1 more source

Cic1p/Nsa3p is required for synthesis and nuclear export of 60S ribosomal subunits [PDF]

open access: yes, 2003
Cic1p/Nsa3p was previously reported to be associated with the 26S proteasome and required for the degradation of specific substrates, but was also shown to be associated with early pre-60S particles and to be localized to the nucleolus.
Tollervey, D   +7 more
core   +1 more source

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